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Article

Mechanisms of mutations inhibiting fusion and infection by Semliki Forest virus.

The Journal of cell biology - 1 Aug 1996

Kielian M, Klimjack M R, Ghosh S, Duffus W A

Abstract excerpt

Semliki Forest virus (SFV) infects cells by an acid-dependent membrane fusion reaction catalyzed by the virus spike protein, a complex containing E1 and E2 transmembrane subunits. E1 carries the putative virus fusion peptide, and mutations in this domain of the spike protein were previously shown...

Topics

Animals
Antibodies, Monoclonal
Antibodies, Viral
Capsid
Cell Fusion
Cell Line
Cricetinae
Hydrogen-Ion Concentration
Kidney
Liposomes
Membrane Fusion
Mutation
Protein Conformation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Semliki forest virus

Trypsin

Viral Envelope Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 8769412
DOI: 10.1083/jcb.134.4.863
PMCID: PMC2120960

Genes

SDS

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8769412-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Mechanisms of mutations inhibiting fusion and infection by Semliki Forest virus.PMID 8769412Read ↗

fus-1, a pH shift mutant of Semliki Forest virus, acts by altering spike subunit interactions via a mutation in the E2 subunit.Semantic proximity Read ↗

Differential roles of two conserved glycine residues in the fusion peptide of Semliki Forest virus.Semantic proximity Read ↗

Role of conserved histidine residues in the low-pH dependence of the Semliki Forest virus fusion protein.Semantic proximity Read ↗

Biosynthesis, maturation, and acid activation of the Semliki Forest virus fusion protein.Semantic proximity Read ↗

The conserved glycine residues in the transmembrane domain of the Semliki Forest virus fusion protein are not required for assembly and fusion.Semantic proximity Read ↗

A conserved histidine in the ij loop of the Semliki Forest virus E1 protein plays an important role in membrane fusion.Semantic proximity Read ↗

A recombinant vesicular stomatitis virus bearing a lethal mutation in the glycoprotein gene uncovers a second site suppressor that restores fusion.Semantic proximity Read ↗

Mutations that promote furin-independent growth of Semliki Forest virus affect p62-E1 interactions and membrane fusion.Semantic proximity Read ↗

Fusion function of the Semliki Forest virus spike is activated by proteolytic cleavage of the envelope glycoprotein precursor p62.Semantic proximity Read ↗

PE2 cleavage mutants of Sindbis virus: correlation between viral infectivity and pH-dependent membrane fusion activation of the spike heterodimer.Semantic proximity Read ↗

An interaction site of the envelope proteins of Semliki Forest virus that is preserved after proteolytic activation.Semantic proximity Read ↗

Spike protein oligomerization control of Semliki Forest virus fusion.Semantic proximity Read ↗

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